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1 The characteristics of the binding of 12‐alpha‐[3H]‐digoxin to the membranes of intact human erythrocytes are described. 2 Only one class of binding site can be demonstrated. Binding is time‐ and temperature‐ dependent, saturable and slowly reversible; it is inhibited by other cardiac glycosides and by potassium. 3 Pre‐incubation with unlabelled digoxin reduces the subsequent binding of 12‐alpha‐[3H] ‐digoxin in stoichiometric fashion. 4 The possible application of the measurement of the binding of 12‐alpha‐[3H]‐digoxin to the study of biochemical pharmacological events occurring during digoxin therapy is discussed. 1979 The British Pharmacological Society

Original publication

DOI

10.1111/j.1365-2125.1979.tb05809.x

Type

Journal article

Journal

British Journal of Clinical Pharmacology

Publication Date

01/01/1979

Volume

8

Pages

115 - 124